01975naa a2200385 a 450000100080000000500110000800800410001910000180006024501720007826000090025052008610025965000150112065000160113565000180115165000150116965000160118465000220120065000100122265000150123265000190124765000170126665000210128365000100130465000190131465000100133365000170134365000260136065300410138670000170142770000190144470000180146370000150148170000170149677300760151315202032023-12-11       1983    bl uuuu     u00u1 u    #d1 aPAGELS, W. R.  aImmunochemical evidence for the involvement of prostaglandin H synthase in hydroperoxide-dependent oxidations by ram seminal vesicle microsomes.h[electronic resource]  c1983  aAbstract: Monoclonal antibodies against prostaglandin H (PGH) synthase have been used to precipitate cyclooxygenase and peroxidase activities from detergent-solubilized preparations of ram seminal vesicle microsomes. Approximately 85% of the solubilized cyclooxygenase activity was precipitated using an excess of anti-PGH synthase antibody; under similar conditions, immunoprecipitation of 60% of the diphenylisobenzofuran peroxidase, 75% of the phenylbutazone peroxidase, and 50% of the epinephrine peroxidase activities occurred. In contrast, less than 10% of the cyclooxygenase or peroxidase activities could be precipitated with nonimmune, control antibody preparations. These data indicate that the hydroperoxidase activity of PGH synthase is the major peroxidase activity catalyzing the co-oxidation of xenobiotics in ram seminal vesicle microsomes.  aAntibodies  aBenzofurans  aEndocrinology  aEnzymology  aEpinephrine  aHydrogen peroxide  aMales  aMicrosomes  aPhenylbutazone  aReproduction  aSeminal vesicles  aSheep  aEndocrinologia  aOvino  aReprodução  aStaphylococcus Aureus  aProstaglandin-Endoperoxide Synthases1 aSACHS, R. J.1 aMARNETT, L. J.1 aDEWITT, D. L.1 aDAY, J. S.1 aSMITH, W. L.  tThe Journal of Biological Chemistrygv. 258, n. 10, p. 6517-6523, 1983.